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2DWS

Cu-containing nitrite reductase at pH 8.4 with bound nitrite

Functional Information from GO Data
ChainGOidnamespacecontents
A0005507molecular_functioncopper ion binding
A0016491molecular_functionoxidoreductase activity
A0019333biological_processdenitrification pathway
A0042128biological_processnitrate assimilation
A0042597cellular_componentperiplasmic space
A0046872molecular_functionmetal ion binding
A0050421molecular_functionnitrite reductase (NO-forming) activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU A 401
ChainResidue
AHIS126
ACYS167
AHIS177
AMET182

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CU A 402
ChainResidue
ANO2501
AASP129
AHIS131
AHIS166
AHIS287
AHIS338

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE NO2 A 501
ChainResidue
AASP129
AHIS131
AHIS166
AHIS287
AILE289
AHIS338
ALEU340
ACU402

Functional Information from PROSITE/UniProt
site_idPS00283
Number of Residues17
DetailsSOYBEAN_KUNITZ Soybean trypsin inhibitor (Kunitz) protease inhibitors family signature. LkDHEGKpVrYDtvYyI
ChainResidueDetails
ALEU194-ILE210

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: type 1 copper site => ECO:0000250
ChainResidueDetails
AHIS126
ACYS167
AHIS177
AMET182

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: type 2 copper site => ECO:0000250
ChainResidueDetails
AHIS131
AHIS166
AHIS338

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1nid
ChainResidueDetails
AGLY97
APHE95

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1nid
ChainResidueDetails
AHIS287
AASP129

227344

PDB entries from 2024-11-13

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